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大鼠骨骼肌磷酸甘油醛脱氢酶的结构研究。

Structural studies on glyceraldehyde-phosphate dehydrogenase from rat skeletal muscle.

作者信息

Nagradova N K, Safronova M I, Baratova L A, Belianova L P

出版信息

Biochim Biophys Acta. 1978 Jan 25;532(1):1-5. doi: 10.1016/0005-2795(78)90441-5.

DOI:10.1016/0005-2795(78)90441-5
PMID:620046
Abstract

The NH2-terminal amino acid sequence of rat skeletal muscle glyceraldehydephosphate dehydrogenase (D-glyceraldehyde-3-phosphate : NAD+ oxidoreductase(physphorylating), EC 1.2.1.12) was determined to be Val-Lys-Val-Gly-Val-Asn-Gly-Phe-Gly-Arg-Ile-Gly-Arg-Leu-Val-Thr-Arg-Ala-Ala-Phe-Ser-Ser-(-)-(-)--Val-Asx-Ile-Val-Ala-Ile. The presence of Asn instead of Asp in position 6 differentiates this enzyme from other glyceraldehyde-3-phosphate dehydrogenases so far sequenced with the exception of the enzymes isolated from liver. The location of Asn in position 6 has been considered as a specific property of liver glyceraldehyde-3-phosphate dehydrogenase (Kulbe, K.D., Jackson, K.W. and Tang, J. (1975) Biochem. Biophys. Res. Commun. 67, 35--42); this suggestion is not sustained by the results of the present investigation. The amino acid composition of the rat skeletal muscle dehydrogenase demonstrates the unusually low histidine content of this enzyme as compared to other mammalian muscle glyceraldehyde-phosphate dehydrogenases.

摘要

已确定大鼠骨骼肌甘油醛-3-磷酸脱氢酶(D-甘油醛-3-磷酸:NAD+氧化还原酶(磷酸化),EC 1.2.1.12)的氨基末端氨基酸序列为Val-Lys-Val-Gly-Val-Asn-Gly-Phe-Gly-Arg-Ile-Gly-Arg-Leu-Val-Thr-Arg-Ala-Ala-Phe-Ser-Ser-(-)-(-)--Val-Asx-Ile-Val-Ala-Ile。第6位存在Asn而非Asp,这使得该酶与迄今测序的其他甘油醛-3-磷酸脱氢酶不同,但从肝脏分离的酶除外。第6位Asn的位置被认为是肝脏甘油醛-3-磷酸脱氢酶的一个特性(库尔贝,K.D.,杰克逊,K.W.和唐,J.(1975年)《生物化学与生物物理学研究通讯》67,35 - 42);本研究结果并不支持这一观点。与其他哺乳动物肌肉甘油醛-3-磷酸脱氢酶相比,大鼠骨骼肌脱氢酶的氨基酸组成表明该酶的组氨酸含量异常低。

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引用本文的文献

1
Identification of an arginine residue important for catalytic activity in the primary structure of D-glyceraldehyde 3-phosphate dehydrogenase. Studies with the rat skeletal-muscle enzyme.鉴定对D-甘油醛-3-磷酸脱氢酶一级结构中催化活性重要的精氨酸残基。对大鼠骨骼肌酶的研究。
Biochem J. 1981 Dec 1;199(3):757-65. doi: 10.1042/bj1990757.